| Abstract |
ABSTRACT
Members of the genus
Mesorhizobium,
which are core components of the rhizosphere and specific symbionts of legume plants, possess genes for acyl-homoserine lactone (AHL) quorum sensing (QS). Here we show
Mesorhizobium japonicum
MAFF 303099 (formerly
M. loti
) synthesizes and responds to
N
-[(2
E
, 4
E
)-2,4-dodecadienoyl] homoserine lactone (2
E,
4
E-
C
12:2
-HSL). We show that the 2
E,
4
E-
C
12:2
-HSL QS circuit involves one of four
luxR-luxI
-type genes found in the sequenced genome of MAFF 303099. We refer to this circuit, which appears to be conserved among
Mesorhizobium
species, as R1-I1. We show that two other
Mesorhizobium
strains also produce 2
E,
4
E-
C
12:2
-HSL. The 2
E,
4
E-
C
12:2
-HSL is unique among known AHLs in its arrangement of two
trans
double bonds. The R1 response to 2
E,
4
E-
C
12:2
-HSL is extremely selective in comparison with other LuxR homologs, and the
trans
double bonds appear critical for R1 signal recognition. Most well-studied LuxI-like proteins use
S
-adenosylmethionine and an acyl-acyl carrier protein as substrates for synthesis of AHLs. Others that form a subgroup of LuxI-type proteins use acyl-coenzyme A substrates rather than acyl-acyl carrier proteins. I1 clusters with the acyl-coenzyme A-type AHL synthases. We show that a gene linked to the
I1
AHL synthase is involved in the production of the QS signal. The discovery of the unique I1 product enforces the view that further study of acyl-coenzyme A-dependent LuxI homologs will expand our knowledge of AHL diversity. The involvement of an additional enzyme in AHL generation leads us to consider this system a three-component QS circuit.
IMPORTANCE
We report a
Mesorhizobium japonicum
quorum sensing (QS) system involving a novel acyl-homoserine lactone (AHL) signal. This system is known to be involved in root nodule symbiosis with host plants. The chemistry of the newly described QS signal indicated that there may be a dedicated cellular enzyme involved in its synthesis in addition to the types known for production of other AHLs. Indeed, we report that an additional gene is required for synthesis of the unique signal, and we propose that this is a three-component QS circuit as opposed to the canonical two-component AHL QS circuits. The signaling system is exquisitely selective. The selectivity may be important when this species resides in the complex microbial communities around host plants and may make this system useful in various synthetic biology applications of QS circuits.
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